PMID: 6172154Dec 15, 1981Paper

Evidence for exchange of inhibitors which bind to the active site of trypsin. Displacement of one inhibitor with a competitive inhibitor

Biochimica Et Biophysica Acta
F S Steven, M M Griffin

Abstract

Two classes of inhibitors of trypsin (ED 3.4.21.4) have been studied, viz. active site-directed agents such as ovomucoid and active site titrants such as 4-methylumbelliferyl-4-guanidinobenzoate. The kinetics of beta-naphthyl-amidase inhibition by an active site-directed agent were markedly different from simultaneous assays of the availability of the active site towards active site titrants in the presence of the active site-directed agents. Analysis of these data indicated an exchange of active site-directed agent by subsequent addition of active site titrant. One class of trypsin inhibitor could be displaced by another from the trypsin active centre. Competitive chase experiments were designed to measure this exchange in which the active site-directed agent was first equilibrated with trypsin, then partially displaced by incremental additions of an active site titrant; the degree of active sites occupied by these two agents was then determined by active site titration with a second reagent.

References

Jan 1, 1976·Methods in Enzymology·P L ColemanE N Shaw
Feb 1, 1978·European Journal of Biochemistry·F S Steven, V Podrazký
Nov 30, 1967·Biochemical and Biophysical Research Communications·T Chase, E Shaw

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Citations

Jan 1, 1984·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·B K Simpson, N F Haard
Aug 1, 1982·European Journal of Biochemistry·F S StevenS Itzhaki

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